1skb
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Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic dynamics
OverviewOverview
Understanding of the atomic movements involved in an enzymatic reaction, needs structural information on the active and inactive native enzyme, molecules and on the enzyme-substrate, enzyme-intermediate, and, enzyme-product(s) complexes. By using the X-ray crystallographic method, four crystal structures of Aspergillus fumigatus phytase were obtained at, resolution higher than 1.7 A. The pH-dependent catalytic activity of A., fumigatus phytase was linked to three water molecules that may prevent the, substrate from binding and thus block nucleophilic attack of the catalytic, imidazole nitrogen. Comparison of various structures also identified the, water molecule that attacks the phosphamide bond during the hydrolysis, process, and established the hydrolysis pathway of the intermediate., Additionally, two reaction product phosphates were observed at the active, site, suggesting a possible product release pathway after hydrolysis of, the intermediate. These results can help explain the catalytic mechanism, throughout the whole acid phosphatase family, as all key residues are, conserved.
About this StructureAbout this Structure
1SKB is a Single protein structure of sequence from Aspergillus fumigatus with NAG and NDG as ligands. Active as 3-phytase, with EC number 3.1.3.8 Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics., Liu Q, Huang Q, Lei XG, Hao Q, Structure. 2004 Sep;12(9):1575-83. PMID:15341723
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